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Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions.

Biotechnol Lett.. 2014-11;

AC Jahns, BHA Rehm. Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North, 4442, New Zealand.

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Abstract

Polyhydroxyalkanoate (PHA) beads, recombinantly produced in Escherichia coli, were functionalized to display lipase B from Candida antarctica as translational protein fusion. The respective beads were characterized in respect to protein content, functionality, long term storage capacity and re-usability. The direct fusion of the PHA synthase, PhaC, to lipase B yielded active PHA lipase beads capable of hydrolyzing glycerol tributyrate. Lipase B beads showed stable activity over several weeks and re-usability without loss of function.

Keywords

Beads; Lipase; PHA synthase (PhaC); Polyhydroxyalkanoate beads

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